Structure of PDB 1h19 Chain A Binding Site BS01

Receptor Information
>1h19 Chain A (length=610) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLR
SLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEI
VIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTP
SVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCY
LIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGP
YVWGQYDLLVLPPSFPYGGMQNPCLTFVTPTLLAGDKSLSNVIAHEISHS
WTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQ
NSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGP
EIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYS
PGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLN
EFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDA
IPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTA
MLVGKDLKVD
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1h19 Chain A Residue 701 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1h19 Leukotriene A4 Hydrolase/Aminopeptidase, Glutamate 271 is a Catalyticresidue with Specific Roles in Two Distinct Enzyme Mechanisms
Resolution2.1 Å
Binding residue
(original residue number in PDB)		H295 H299 E318
Binding residue
(residue number reindexed from 1)		H295 H299 E318
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Q271 H295 E296 H299 E318 D375 Y383
Catalytic site (residue number reindexed from 1) Q271 H295 E296 H299 E318 D375 Y383
Enzyme Commision number 3.3.2.6: leukotriene-A4 hydrolase.
3.4.11.4: tripeptide aminopeptidase.
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0004177 aminopeptidase activity
GO:0004301 epoxide hydrolase activity
GO:0004463 leukotriene-A4 hydrolase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0045148 tripeptide aminopeptidase activity
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0006629 lipid metabolic process
GO:0006691 leukotriene metabolic process
GO:0010043 response to zinc ion
GO:0019370 leukotriene biosynthetic process
GO:0019538 protein metabolic process
GO:0043171 peptide catabolic process
GO:0043434 response to peptide hormone
GO:0060509 type I pneumocyte differentiation
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome
GO:1904724 tertiary granule lumen
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h19, PDBe:1h19, PDBj:1h19
PDBsum1h19
PubMed11675384
UniProtP09960|LKHA4_HUMAN Leukotriene A-4 hydrolase (Gene Name=LTA4H)

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